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38  structures 104  species 2  interactions 421  sequences 8  architectures

Family: Stathmin (PF00836)

Summary: Stathmin family

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This is the Wikipedia entry entitled "Stathmin protein domain". More...

Stathmin protein domain Edit Wikipedia article

PDB 1z2b EBI.jpg
Structure of Tubulin-Colchicine-Vinblastine: Stathmin-like domain complex
Symbol Stathmin
Pfam PF00836
InterPro IPR000956
SCOP 1sa0

In molecular biology, the protein domain, Stathmin is a crucial protein that regulates the cell cytoskeleton. Changes in the cytoskeleton are important because the cytoskeleton is a scaffold required for many cellular processes, such as cytoplasmic organization, cell division and cell motility.[1] More specifically, stathmin is crucial in regulating the cell cycle.[2] It is found solely in eukaryotes


The function of Stathmin is to regulate the cytoskeleton of the cell. The cytoskeleton is made up of long hollow cylinders named microtubules. These microtubules are made up of alpha and beta tubulin heterodimers. The changes in cytoskeleton are known as microtubule dynamics; the addition of the tubulin subunits lead to polymerisation and their loss, depolymerisation.[1] Stathmin regulates these by promoting depolymerization of microtubules or preventing polymerization of tubulin heterodimers.[2]

Additionally, Stathmin is thought to have a role in cell signaling pathway. Stathmin is a ubiquitous phosphorylated protein which makes it act as an intracellular relay for diverse regulatory pathways,[3] functioning through a variety of second messengers.

Its phosphorylation and gene expression are regulated throughout development [4] and in response to extracellular signals regulating cell proliferation, differentiation and function.[5]


Stathmin, and the related proteins SCG10 and XB3, contain a N-terminal domain (XB3 contains an additional N-terminal hydrophobic region), a 78 amino acid coiled-coil region, and a short C-terminal domain.


  1. ^ a b Kueh HY, Mitchison TJ (August 2009). "Structural plasticity in actin and tubulin polymer dynamics". Science 325 (5943): 960–3. doi:10.1126/science.1168823. PMC 2864651. PMID 19696342. 
  2. ^ a b Rubin CI, Atweh GF (October 2004). "The role of stathmin in the regulation of the cell cycle". J. Cell. Biochem. 93 (2): 242–50. doi:10.1002/jcb.20187. PMID 15368352. 
  3. ^ Maucuer A, Doye V, Sobel A (May 1990). "A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations". FEBS Lett. 264 (2): 275–8. doi:10.1016/0014-5793(90)80266-L. PMID 2358074. 
  4. ^ Maucuer A, Moreau J, Méchali M, Sobel A (August 1993). "Stathmin gene family: phylogenetic conservation and developmental regulation in Xenopus". J. Biol. Chem. 268 (22): 16420–9. PMID 8344928. 
  5. ^ Doye V, Soubrier F, Bauw G, Boutterin MC, Beretta L, Koppel J, Vandekerckhove J, Sobel A (July 1989). "A single cDNA encodes two isoforms of stathmin, a developmentally regulated neuron-enriched phosphoprotein". J. Biol. Chem. 264 (21): 12134–7. PMID 2745432. 

This article incorporates text from the public domain Pfam and InterPro IPR000956

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Stathmin family Provide feedback

The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerisation of tubulin heterodimers [1].

Literature references

  1. Rubin CI, Atweh GF; , J Cell Biochem 2004;93:242-250.: The role of stathmin in the regulation of the cell cycle. PUBMED:15368352 EPMC:15368352

  2. Gigant B, Curmi PA, Martin-Barbey C, Charbaut E, Lachkar S, Lebeau L, Siavoshian S, Sobel A, Knossow M; , Cell 2000;102:809-816.: The 4 A X-ray structure of a tubulin:stathmin-like domain complex. PUBMED:11030624 EPMC:11030624

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000956

Stathmin [PUBMED:1957351] (from the Greek 'stathmos' which means relay), is a ubiquitous intracellular protein, present in a variety of phosphorylated forms. It is involved in the regulation of the microtubule (MT) filament system by destabilising microtubules. It prevents assembly and promotes disassembly of microtubules [PUBMED:14598370]. However, when phosphorylated, its destabilisation ability is significantly reduced [PUBMED:11160824].

The stathmin family also includes:

  • Stathmin 2 (Protein SCG10); a neuron-specific, membrane-associated protein that accumulates in the growth cones of developing neurons. It is highly similar in its sequence to stathmin, but differs in that it contains an additional N-terminal hydrophobic segment of 32 residues which is probably responsible for its interaction with membranes.
  • Stathmin 3 (SCG10-like protein; SCLIP) [PUBMED:9603203]; a protein specifically expressed in neurons.
  • Stathmin 4 (Stathmin-like protein B3); which contains an additional N- terminal hydrophobic domain [PUBMED:9342231].

These proteins possess a stathmin-like domain (SLD) with various N-terminal extensions. SLD is a highly conserved domain of 149 amino acid residues. Structurally, it consists of an N-terminal domain of about 45 residues followed by a 78 residue alpha-helical domain consisting of a heptad repeat coiled coil structure and a C-terminal domain of 25 residues [PUBMED:15014504, PUBMED:11278715]. The SLD binds two tubulins arranged longitudinally, head-to-tail, in protofilament-like complexes.

Gene Ontology

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Domain organisation

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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_1551 (release 2.1)
Previous IDs: none
Type: Family
Author: Bateman A, Mistry J, Segerman B
Number in seed: 30
Number in full: 421
Average length of the domain: 122.80 aa
Average identity of full alignment: 48 %
Average coverage of the sequence by the domain: 62.25 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.5 21.5
Trusted cut-off 21.5 21.5
Noise cut-off 21.4 21.4
Model length: 136
Family (HMM) version: 16
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Species distribution

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There are 2 interactions for this family. More...

Tubulin_C Tubulin


For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Stathmin domain has been found. There are 38 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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